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P19971

- TYPH_HUMAN

UniProt

P19971 - TYPH_HUMAN

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Protein

Thymidine phosphorylase

Gene

TYMP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro.1 Publication
Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.1 Publication

Catalytic activityi

Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate
Binding sitei202 – 2021Substrate
Binding sitei217 – 2171Substrate
Binding sitei221 – 2211Substrate

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. platelet-derived growth factor receptor binding Source: ProtInc
  3. pyrimidine-nucleoside phosphorylase activity Source: InterPro
  4. thymidine phosphorylase activity Source: ProtInc
  5. transferase activity, transferring pentosyl groups Source: Reactome

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. chemotaxis Source: UniProtKB-KW
  4. DNA replication Source: ProtInc
  5. mitochondrial genome maintenance Source: ProtInc
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. pyrimidine nucleobase metabolic process Source: Reactome
  8. pyrimidine nucleoside catabolic process Source: Reactome
  9. pyrimidine nucleoside salvage Source: Reactome
  10. pyrimidine nucleotide metabolic process Source: ProtInc
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Growth factor, Transferase

Keywords - Biological processi

Angiogenesis, Chemotaxis, Differentiation

Enzyme and pathway databases

BioCyciMetaCyc:HS00442-MONOMER.
BRENDAi2.4.2.4. 2681.
ReactomeiREACT_1023. Pyrimidine catabolism.
REACT_655. Pyrimidine salvage reactions.
SABIO-RKP19971.
UniPathwayiUPA00578; UER00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine phosphorylase (EC:2.4.2.4)
Short name:
TP
Alternative name(s):
Gliostatin
Platelet-derived endothelial cell growth factor
Short name:
PD-ECGF
TdRPase
Gene namesi
Name:TYMP
Synonyms:ECGF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:3148. TYMP.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Mitochondrial DNA depletion syndrome 1, MNGIE type (MTDPS1) [MIM:603041]: A multisystem disease associated with mitochondrial dysfunction. It is clinically characterized by onset between the second and fifth decades of life, ptosis, progressive external ophthalmoplegia, gastrointestinal dysmotility (often pseudoobstruction), diffuse leukoencephalopathy, cachexia, peripheral neuropathy, and myopathy.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441R → Q in MTDPS1. 1 Publication
VAR_016777
Natural varianti145 – 1451G → R in MTDPS1. 1 Publication
VAR_007643
Natural varianti153 – 1531G → S in MTDPS1. 1 Publication
VAR_007644
Natural varianti222 – 2221K → R in MTDPS1. 1 Publication
VAR_007645
Natural varianti289 – 2891E → A in MTDPS1. 1 Publication
VAR_007646
Natural varianti397 – 3982Missing in MTDPS1. 1 Publication
VAR_007647

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991Y → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi199 – 1991Y → F: Reduced catalytic activity. 1 Publication
Mutagenesisi199 – 1991Y → L: Reduced catalytic activity. 1 Publication

Keywords - Diseasei

Disease mutation, Progressive external ophthalmoplegia

Organism-specific databases

MIMi603041. phenotype.
Orphaneti298. Mitochondrial neurogastrointestinal encephalomyopathy.
PharmGKBiPA162407502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1010PRO_0000035874
Chaini11 – 482472Thymidine phosphorylasePRO_0000035875Add
BLAST

Proteomic databases

MaxQBiP19971.
PaxDbiP19971.
PRIDEiP19971.

2D gel databases

OGPiP19971.

PTM databases

PhosphoSiteiP19971.

Expressioni

Gene expression databases

BgeeiP19971.
CleanExiHS_TYMP.
ExpressionAtlasiP19971. baseline and differential.
GenevestigatoriP19971.

Organism-specific databases

HPAiCAB002518.
HPA001072.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi108219. 15 interactions.
IntActiP19971. 1 interaction.
STRINGi9606.ENSP00000252029.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 449
Helixi51 – 6313
Helixi68 – 8114
Helixi85 – 9612
Helixi106 – 1116
Beta strandi112 – 1187
Helixi125 – 13410
Turni135 – 1373
Beta strandi139 – 1435
Helixi154 – 1585
Helixi170 – 18011
Beta strandi181 – 1855
Beta strandi189 – 1924
Helixi193 – 20412
Helixi211 – 22414
Beta strandi228 – 2369
Beta strandi240 – 2445
Helixi245 – 26117
Beta strandi266 – 2727
Beta strandi280 – 2834
Helixi284 – 29411
Helixi300 – 31617
Beta strandi319 – 3224
Helixi323 – 33513
Helixi338 – 34912
Helixi354 – 3629
Helixi365 – 3717
Beta strandi376 – 3827
Beta strandi387 – 3926
Helixi394 – 40512
Beta strandi409 – 4124
Beta strandi420 – 4234
Beta strandi436 – 44611
Helixi449 – 45810
Beta strandi459 – 4646
Beta strandi475 – 4773

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UOUX-ray2.11A12-482[»]
2J0FX-ray2.31A/B/C/D1-482[»]
2WK5X-ray2.99A/B/C/D1-482[»]
2WK6X-ray2.50A/B1-482[»]
ProteinModelPortaliP19971.
SMRiP19971. Positions 32-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19971.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati265 – 27915R-V-A-A-A-L-X(5,6)-L-G-RAdd
BLAST
Repeati329 – 34214R-V-A-A-A-L-X(5,6)-L-G-RAdd
BLAST
Repeati393 – 4019R-A-L-X-X-A-L-V-L
Repeati453 – 4619R-A-L-X-X-A-L-V-L

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0213.
GeneTreeiENSGT00390000009250.
HOGENOMiHOG000047313.
HOVERGENiHBG000082.
InParanoidiP19971.
KOiK00758.
OMAiNVGHTLE.
OrthoDBiEOG744T97.
PhylomeDBiP19971.
TreeFamiTF332198.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
InterProiIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
[Graphical view]
PANTHERiPTHR10515. PTHR10515. 1 hit.
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000478. TP_PyNP. 1 hit.
SMARTiSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsiTIGR02644. Y_phosphoryl. 1 hit.
PROSITEiPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P19971-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAALMTPGTG APPAPGDFSG EGSQGLPDPS PEPKQLPELI RMKRDGGRLS
60 70 80 90 100
EADIRGFVAA VVNGSAQGAQ IGAMLMAIRL RGMDLEETSV LTQALAQSGQ
110 120 130 140 150
QLEWPEAWRQ QLVDKHSTGG VGDKVSLVLA PALAACGCKV PMISGRGLGH
160 170 180 190 200
TGGTLDKLES IPGFNVIQSP EQMQVLLDQA GCCIVGQSEQ LVPADGILYA
210 220 230 240 250
ARDVTATVDS LPLITASILS KKLVEGLSAL VVDVKFGGAA VFPNQEQARE
260 270 280 290 300
LAKTLVGVGA SLGLRVAAAL TAMDKPLGRC VGHALEVEEA LLCMDGAGPP
310 320 330 340 350
DLRDLVTTLG GALLWLSGHA GTQAQGAARV AAALDDGSAL GRFERMLAAQ
360 370 380 390 400
GVDPGLARAL CSGSPAERRQ LLPRAREQEE LLAPADGTVE LVRALPLALV
410 420 430 440 450
LHELGAGRSR AGEPLRLGVG AELLVDVGQR LRRGTPWLRV HRDGPALSGP
460 470 480
QSRALQEALV LSDRAPFAAP SPFAELVLPP QQ
Length:482
Mass (Da):49,955
Last modified:June 7, 2005 - v2
Checksum:i0652FA0B8F3BDE28
GO
Isoform 2 (identifier: P19971-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     386-386: D → DAPLPA

Note: No experimental confirmation available.

Show »
Length:487
Mass (Da):50,405
Checksum:iC2F16246C51DCE00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951D → E in AAH18160. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441R → Q in MTDPS1. 1 Publication
VAR_016777
Natural varianti145 – 1451G → R in MTDPS1. 1 Publication
VAR_007643
Natural varianti153 – 1531G → S in MTDPS1. 1 Publication
VAR_007644
Natural varianti222 – 2221K → R in MTDPS1. 1 Publication
VAR_007645
Natural varianti289 – 2891E → A in MTDPS1. 1 Publication
VAR_007646
Natural varianti397 – 3982Missing in MTDPS1. 1 Publication
VAR_007647
Natural varianti471 – 4711S → L.2 Publications
Corresponds to variant rs11479 [ dbSNP | Ensembl ].
VAR_007648

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei386 – 3861D → DAPLPA in isoform 2. 1 PublicationVSP_045556

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63193 mRNA. Translation: AAA60043.1.
AK225269 mRNA. No translation available.
U62317 Genomic DNA. Translation: AAB03344.2.
BC018160 mRNA. Translation: AAH18160.1.
BC052211 mRNA. Translation: AAH52211.1.
CCDSiCCDS14096.1. [P19971-1]
CCDS58811.1. [P19971-2]
PIRiS03904.
RefSeqiNP_001107227.1. NM_001113755.2. [P19971-1]
NP_001107228.1. NM_001113756.2. [P19971-1]
NP_001244917.1. NM_001257988.1. [P19971-1]
NP_001244918.1. NM_001257989.1. [P19971-2]
NP_001944.1. NM_001953.4. [P19971-1]
UniGeneiHs.180903.
Hs.730607.

Genome annotation databases

EnsembliENST00000252029; ENSP00000252029; ENSG00000025708. [P19971-1]
ENST00000395678; ENSP00000379036; ENSG00000025708. [P19971-1]
ENST00000395680; ENSP00000379037; ENSG00000025708. [P19971-1]
ENST00000395681; ENSP00000379038; ENSG00000025708. [P19971-2]
ENST00000613148; ENSP00000477950; ENSG00000025708. [P19971-1]
GeneIDi1890.
KEGGihsa:1890.
UCSCiuc003bmb.5. human. [P19971-1]

Polymorphism databases

DMDMi67477361.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

R&D Systems' cytokine mini-reviews: PD-ECGF
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63193 mRNA. Translation: AAA60043.1 .
AK225269 mRNA. No translation available.
U62317 Genomic DNA. Translation: AAB03344.2 .
BC018160 mRNA. Translation: AAH18160.1 .
BC052211 mRNA. Translation: AAH52211.1 .
CCDSi CCDS14096.1. [P19971-1 ]
CCDS58811.1. [P19971-2 ]
PIRi S03904.
RefSeqi NP_001107227.1. NM_001113755.2. [P19971-1 ]
NP_001107228.1. NM_001113756.2. [P19971-1 ]
NP_001244917.1. NM_001257988.1. [P19971-1 ]
NP_001244918.1. NM_001257989.1. [P19971-2 ]
NP_001944.1. NM_001953.4. [P19971-1 ]
UniGenei Hs.180903.
Hs.730607.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UOU X-ray 2.11 A 12-482 [» ]
2J0F X-ray 2.31 A/B/C/D 1-482 [» ]
2WK5 X-ray 2.99 A/B/C/D 1-482 [» ]
2WK6 X-ray 2.50 A/B 1-482 [» ]
ProteinModelPortali P19971.
SMRi P19971. Positions 32-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108219. 15 interactions.
IntActi P19971. 1 interaction.
STRINGi 9606.ENSP00000252029.

Chemistry

BindingDBi P19971.
ChEMBLi CHEMBL3106.
DrugBanki DB01101. Capecitabine.
DB00369. Cidofovir.
DB00322. Floxuridine.
DB00544. Fluorouracil.
DB00432. Trifluridine.

PTM databases

PhosphoSitei P19971.

Polymorphism databases

DMDMi 67477361.

2D gel databases

OGPi P19971.

Proteomic databases

MaxQBi P19971.
PaxDbi P19971.
PRIDEi P19971.

Protocols and materials databases

DNASUi 1890.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252029 ; ENSP00000252029 ; ENSG00000025708 . [P19971-1 ]
ENST00000395678 ; ENSP00000379036 ; ENSG00000025708 . [P19971-1 ]
ENST00000395680 ; ENSP00000379037 ; ENSG00000025708 . [P19971-1 ]
ENST00000395681 ; ENSP00000379038 ; ENSG00000025708 . [P19971-2 ]
ENST00000613148 ; ENSP00000477950 ; ENSG00000025708 . [P19971-1 ]
GeneIDi 1890.
KEGGi hsa:1890.
UCSCi uc003bmb.5. human. [P19971-1 ]

Organism-specific databases

CTDi 1890.
GeneCardsi GC22M050964.
GeneReviewsi TYMP.
HGNCi HGNC:3148. TYMP.
HPAi CAB002518.
HPA001072.
MIMi 131222. gene.
603041. phenotype.
neXtProti NX_P19971.
Orphaneti 298. Mitochondrial neurogastrointestinal encephalomyopathy.
PharmGKBi PA162407502.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0213.
GeneTreei ENSGT00390000009250.
HOGENOMi HOG000047313.
HOVERGENi HBG000082.
InParanoidi P19971.
KOi K00758.
OMAi NVGHTLE.
OrthoDBi EOG744T97.
PhylomeDBi P19971.
TreeFami TF332198.

Enzyme and pathway databases

UniPathwayi UPA00578 ; UER00638 .
BioCyci MetaCyc:HS00442-MONOMER.
BRENDAi 2.4.2.4. 2681.
Reactomei REACT_1023. Pyrimidine catabolism.
REACT_655. Pyrimidine salvage reactions.
SABIO-RK P19971.

Miscellaneous databases

EvolutionaryTracei P19971.
GeneWikii ECGF1.
GenomeRNAii 1890.
NextBioi 7707.
PROi P19971.
SOURCEi Search...

Gene expression databases

Bgeei P19971.
CleanExi HS_TYMP.
ExpressionAtlasi P19971. baseline and differential.
Genevestigatori P19971.

Family and domain databases

Gene3Di 3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
InterProi IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
[Graphical view ]
PANTHERi PTHR10515. PTHR10515. 1 hit.
Pfami PF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000478. TP_PyNP. 1 hit.
SMARTi SM00941. PYNP_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsi TIGR02644. Y_phosphoryl. 1 hit.
PROSITEi PS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor."
    Ishikawa F., Miyazono K., Hellman U., Drexler H., Wernstedt C., Hagiwara K., Usuki K., Takaku F., Risau W., Heldin C.-H.
    Nature 338:557-562(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT LEU-471.
    Tissue: Placenta.
  2. "Expression of recombinant platelet-derived endothelial cell growth factor in the yeast Saccharomyces cerevisiae."
    Finnis C., Goodey A., Courtney M., Sleep D.
    Yeast 8:57-60(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Dermoid cancer.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-471.
    Tissue: Brain and Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE OF 149-244, PROTEIN SEQUENCE OF 125-178 AND 236-244.
  7. "Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor."
    Asai K., Nakanishi K., Isobe I., Eksioglu Y.Z., Hirano A., Hama K., Miyamoto T., Kato T.
    J. Biol. Chem. 267:20311-20316(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  8. "Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity."
    Usuki K., Saras J., Waltenberger J., Miyazono K., Pierce G., Thomason A., Heldin C.-H.
    Biochem. Biophys. Res. Commun. 184:1311-1316(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 12-482 IN COMPLEX WITH INHIBITOR, SUBUNIT.
  11. "Structural basis for non-competitive product inhibition in human thymidine phosphorylase: implications for drug design."
    El Omari K., Bronckaers A., Liekens S., Perez-Perez M.J., Balzarini J., Stammers D.K.
    Biochem. J. 399:199-204(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), SUBUNIT.
  12. "Structures of native human thymidine phosphorylase and in complex with 5-iodouracil."
    Mitsiki E., Papageorgiou A.C., Iyer S., Thiyagarajan N., Prior S.H., Sleep D., Finnis C., Acharya K.R.
    Biochem. Biophys. Res. Commun. 386:666-670(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH 5-IODOURACIL, SUBSTRATE-BINDING SITES, MUTAGENESIS OF TYR-199.
  13. "Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder."
    Nishino I., Spinazzola A., Hirano M.
    Science 283:689-692(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MTDPS1 ARG-145; SER-153; ARG-222; ALA-289 AND 397-LEU-ALA-398 DEL.
  14. Cited for: VARIANT MTDPS1 GLN-44.

Entry informationi

Entry nameiTYPH_HUMAN
AccessioniPrimary (citable) accession number: P19971
Secondary accession number(s): A8MW15
, H9KVA0, Q13390, Q8WVB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 7, 2005
Last modified: October 29, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3